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Conserved domains on  [gi|499349865|ref|WP_011039158|]
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glutamine amidotransferase [Xanthomonas campestris]

Protein Classification

glutamine amidotransferase( domain architecture ID 10793139)

glutamine amidotransferase (GATase) catalyzes the transfer of ammonia from the amide side chain of glutamine to an acceptor substrate

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
PRK09065 PRK09065
glutamine amidotransferase; Provisional
 3-237 4.96e-139

glutamine amidotransferase; Provisional


:

Pssm-ID: 181635 [Multi-domain]  Cd Length: 237  Bit Score: 390.09  E-value: 4.96e-139
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499349865   3 ALPFLIIETGHPVSGMK-QYGRFPHWIRVAAGLAERETVVIDVANGDRLPDRRGFAGTLISGSAAFVTDRADWSERSAEW 81
Cdd:PRK09065   1 VKPLLIIQTGTPPPSIRaRYGDFPHWIRVALGLAEQPVVVVRVFAGEPLPAPDDFAGVIITGSWAMVTDRLDWSERTADW 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499349865  82 LRDAAHAGMPLLGICYGHQLIAHALGGQVDYNPAGRESGTIALELHPPAHEDPLFAGLPPQFPAHATHLQTVLRAPDGAV 161
Cdd:PRK09065  81 LRQAAAAGMPLLGICYGHQLLAHALGGEVGYNPAGRESGTVTVELHPAAADDPLFAGLPAQFPAHLTHLQSVLRLPPGAV 160

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 499349865 162 VLARSPQDQCHAFRWGQSTWGVQFHPEFATHHMRGYVRARADCIARHGRCARTVASEVSAAPMARKLLRRFVHHAR 237
Cdd:PRK09065 161 VLARSAQDPHQAFRYGPHAWGVQFHPEFTAHIMRAYLRARADCLRREGLDARTLLREVSEAPWARKLLRRFVRLAR 236
 
Name Accession Description Interval E-value
PRK09065 PRK09065
glutamine amidotransferase; Provisional
 3-237 4.96e-139

glutamine amidotransferase; Provisional


Pssm-ID: 181635 [Multi-domain]  Cd Length: 237  Bit Score: 390.09  E-value: 4.96e-139
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499349865   3 ALPFLIIETGHPVSGMK-QYGRFPHWIRVAAGLAERETVVIDVANGDRLPDRRGFAGTLISGSAAFVTDRADWSERSAEW 81
Cdd:PRK09065   1 VKPLLIIQTGTPPPSIRaRYGDFPHWIRVALGLAEQPVVVVRVFAGEPLPAPDDFAGVIITGSWAMVTDRLDWSERTADW 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499349865  82 LRDAAHAGMPLLGICYGHQLIAHALGGQVDYNPAGRESGTIALELHPPAHEDPLFAGLPPQFPAHATHLQTVLRAPDGAV 161
Cdd:PRK09065  81 LRQAAAAGMPLLGICYGHQLLAHALGGEVGYNPAGRESGTVTVELHPAAADDPLFAGLPAQFPAHLTHLQSVLRLPPGAV 160

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 499349865 162 VLARSPQDQCHAFRWGQSTWGVQFHPEFATHHMRGYVRARADCIARHGRCARTVASEVSAAPMARKLLRRFVHHAR 237
Cdd:PRK09065 161 VLARSAQDPHQAFRYGPHAWGVQFHPEFTAHIMRAYLRARADCLRREGLDARTLLREVSEAPWARKLLRRFVRLAR 236
GuaA1 COG0518
GMP synthase, glutamine amidotransferase domain [Nucleotide transport and metabolism]; GMP ...
 5-236 2.77e-65

GMP synthase, glutamine amidotransferase domain [Nucleotide transport and metabolism]; GMP synthase, glutamine amidotransferase domain is part of the Pathway/BioSystem: Purine biosynthesis


Pssm-ID: 440284 [Multi-domain]  Cd Length: 225  Bit Score: 202.48  E-value: 2.77e-65
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499349865   5 PFLIIETGHpvsgmkQYGRFPHWIRVAAGLAERETVVIDVANGDRLPDR---RGFAGTLISGSAAFVTDRADWSERSAEW 81
Cdd:COG0518    1 KILILDHDP------FGGQYPGLIARRLREAGIELDVLRVYAGEILPYDpdlEDPDGLILSGGPMSVYDEDPWLEDEPAL 74

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499349865  82 LRDAAHAGMPLLGICYGHQLIAHALGGQVDYNPaGRESGTIALELHPpahEDPLFAGLPPQFPAHATHLQTVLRAPDGAV 161
Cdd:COG0518   75 IREAFELGKPVLGICYGAQLLAHALGGKVEPGP-GREIGWAPVELTE---ADPLFAGLPDEFTVWMSHGDTVTELPEGAE 150

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 499349865 162 VLARSPQDQCHAFRWGQSTWGVQFHPEFATHHMRGYVRARADCIARHGRCARTVASEVSAAPMARKLLRRFVHHA 236
Cdd:COG0518  151 VLASSDNCPNQAFRYGRRVYGVQFHPEVTHTMMEAWLEERADELAAEELLAEASLHDPELREAGRRLLRNFLREI 225
GATase1_1 cd01741
Subgroup of proteins having the Type 1 glutamine amidotransferase (GATase1) domain; This group ...
 5-188 7.71e-61

Subgroup of proteins having the Type 1 glutamine amidotransferase (GATase1) domain; This group contains a subgroup of proteins having the Type 1 glutamine amidotransferase (GATase1) domain. GATase activity catalyses the transfer of ammonia from the amide side chain of glutamine to an acceptor substrate. Glutamine amidotransferases (GATase) includes the triad family of amidotransferases which have a conserved Cys-His-Glu catalytic triad in the glutaminase active site. In this subgroup this triad is conserved. GATase activity can be found in a range of biosynthetic enzymes, including: glutamine amidotransferase, formylglycinamide ribonucleotide, GMP synthetase , anthranilate synthase component II, glutamine-dependent carbamoyl phosphate synthase, cytidine triphosphate synthetase, gamma-glutamyl hydrolase, imidazole glycerol phosphate synthase and, cobyric acid synthase. Glutamine amidotransferase (GATase) domains can occur either as single polypeptides, as in glutamine amidotransferases, or as domains in a much larger multifunctional synthase protein, such as CPSase.


Pssm-ID: 153212 [Multi-domain]  Cd Length: 188  Bit Score: 189.76  E-value: 7.71e-61
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499349865   5 PFLIIETGHPVSGmkqyGRFPHWIRvAAGLAERETVVIDVANGDRLPDRRGFAGTLISGSAAFV-TDRADWSERSAEWLR 83
Cdd:cd01741    1 RILILQHDTPEGP----GLFEDLLR-EAGAETIEIDVVDVYAGELLPDLDDYDGLVILGGPMSVdEDDYPWLKKLKELIR 75

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499349865  84 DAAHAGMPLLGICYGHQLIAHALGGQVDYNPAGRESGTIALELHPPAHEDPLFAGLPPQFPAHATHLQTVLRAPDGAVVL 163
Cdd:cd01741   76 QALAAGKPVLGICLGHQLLARALGGKVGRNPKGWEIGWFPVTLTEAGKADPLFAGLPDEFPVFHWHGDTVVELPPGAVLL 155

                        170       180
                 ....*....|....*....|....*
gi 499349865 164 ARSPQDQCHAFRWGQSTWGVQFHPE 188
Cdd:cd01741  156 ASSEACPNQAFRYGDRALGLQFHPE 180
guaA_Nterm TIGR00888
GMP synthase (glutamine-hydrolyzing), N-terminal domain or A subunit; This protein of purine ...
 57-188 7.19e-27

GMP synthase (glutamine-hydrolyzing), N-terminal domain or A subunit; This protein of purine de novo biosynthesis is well-conserved. However, it appears to split into two separate polypeptide chains in most of the Archaea. This N-terminal region would be the smaller subunit. [Purines, pyrimidines, nucleosides, and nucleotides, Purine ribonucleotide biosynthesis]


Pssm-ID: 129966 [Multi-domain]  Cd Length: 188  Bit Score: 102.39  E-value: 7.19e-27
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499349865   57 AGTLISGSAAFVtdradWSERSAEWLRDAAHAGMPLLGICYGHQLIAHALGGQVDYNPAgRESGTIALELhppAHEDPLF 136
Cdd:TIGR00888  43 KGIILSGGPSSV-----YAENAPRADEKIFELGVPVLGICYGMQLMAKQLGGEVGRAEK-REYGKAELEI---LDEDDLF 113

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|...
gi 499349865  137 AGLPPQFPAHATHLQTVLRAPDGAVVLARSPQDQCHAFR-WGQSTWGVQFHPE 188
Cdd:TIGR00888 114 RGLPDESTVWMSHGDKVKELPEGFKVLATSDNCPVAAMAhEEKPIYGVQFHPE 166
GATase pfam00117
Glutamine amidotransferase class-I;
82-189 4.10e-13

Glutamine amidotransferase class-I;


Pssm-ID: 395067 [Multi-domain]  Cd Length: 188  Bit Score: 65.72  E-value: 4.10e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499349865   82 LRDAAHAGMPLLGICYGHQLIAHALGGQVDynPAGRES---GTIALELHPPAhedpLFAGLPPQFPAHATHLQTV--LRA 156
Cdd:pfam00117  63 IREARELKIPILGICLGHQLLALAFGGKVV--KAKKFGhhgKNSPVGDDGCG----LFYGLPNVFIVRRYHSYAVdpDTL 136

                          90       100       110
                  ....*....|....*....|....*....|....*
gi 499349865  157 PDGAVVLARSPQDQC-HAFRWGQSTW-GVQFHPEF 189
Cdd:pfam00117 137 PDGLEVTATSENDGTiMGIRHKKLPIfGVQFHPES 171
 
Name Accession Description Interval E-value
PRK09065 PRK09065
glutamine amidotransferase; Provisional
 3-237 4.96e-139

glutamine amidotransferase; Provisional


Pssm-ID: 181635 [Multi-domain]  Cd Length: 237  Bit Score: 390.09  E-value: 4.96e-139
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499349865   3 ALPFLIIETGHPVSGMK-QYGRFPHWIRVAAGLAERETVVIDVANGDRLPDRRGFAGTLISGSAAFVTDRADWSERSAEW 81
Cdd:PRK09065   1 VKPLLIIQTGTPPPSIRaRYGDFPHWIRVALGLAEQPVVVVRVFAGEPLPAPDDFAGVIITGSWAMVTDRLDWSERTADW 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499349865  82 LRDAAHAGMPLLGICYGHQLIAHALGGQVDYNPAGRESGTIALELHPPAHEDPLFAGLPPQFPAHATHLQTVLRAPDGAV 161
Cdd:PRK09065  81 LRQAAAAGMPLLGICYGHQLLAHALGGEVGYNPAGRESGTVTVELHPAAADDPLFAGLPAQFPAHLTHLQSVLRLPPGAV 160

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 499349865 162 VLARSPQDQCHAFRWGQSTWGVQFHPEFATHHMRGYVRARADCIARHGRCARTVASEVSAAPMARKLLRRFVHHAR 237
Cdd:PRK09065 161 VLARSAQDPHQAFRYGPHAWGVQFHPEFTAHIMRAYLRARADCLRREGLDARTLLREVSEAPWARKLLRRFVRLAR 236
GuaA1 COG0518
GMP synthase, glutamine amidotransferase domain [Nucleotide transport and metabolism]; GMP ...
 5-236 2.77e-65

GMP synthase, glutamine amidotransferase domain [Nucleotide transport and metabolism]; GMP synthase, glutamine amidotransferase domain is part of the Pathway/BioSystem: Purine biosynthesis


Pssm-ID: 440284 [Multi-domain]  Cd Length: 225  Bit Score: 202.48  E-value: 2.77e-65
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499349865   5 PFLIIETGHpvsgmkQYGRFPHWIRVAAGLAERETVVIDVANGDRLPDR---RGFAGTLISGSAAFVTDRADWSERSAEW 81
Cdd:COG0518    1 KILILDHDP------FGGQYPGLIARRLREAGIELDVLRVYAGEILPYDpdlEDPDGLILSGGPMSVYDEDPWLEDEPAL 74

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499349865  82 LRDAAHAGMPLLGICYGHQLIAHALGGQVDYNPaGRESGTIALELHPpahEDPLFAGLPPQFPAHATHLQTVLRAPDGAV 161
Cdd:COG0518   75 IREAFELGKPVLGICYGAQLLAHALGGKVEPGP-GREIGWAPVELTE---ADPLFAGLPDEFTVWMSHGDTVTELPEGAE 150

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 499349865 162 VLARSPQDQCHAFRWGQSTWGVQFHPEFATHHMRGYVRARADCIARHGRCARTVASEVSAAPMARKLLRRFVHHA 236
Cdd:COG0518  151 VLASSDNCPNQAFRYGRRVYGVQFHPEVTHTMMEAWLEERADELAAEELLAEASLHDPELREAGRRLLRNFLREI 225
GATase1_1 cd01741
Subgroup of proteins having the Type 1 glutamine amidotransferase (GATase1) domain; This group ...
 5-188 7.71e-61

Subgroup of proteins having the Type 1 glutamine amidotransferase (GATase1) domain; This group contains a subgroup of proteins having the Type 1 glutamine amidotransferase (GATase1) domain. GATase activity catalyses the transfer of ammonia from the amide side chain of glutamine to an acceptor substrate. Glutamine amidotransferases (GATase) includes the triad family of amidotransferases which have a conserved Cys-His-Glu catalytic triad in the glutaminase active site. In this subgroup this triad is conserved. GATase activity can be found in a range of biosynthetic enzymes, including: glutamine amidotransferase, formylglycinamide ribonucleotide, GMP synthetase , anthranilate synthase component II, glutamine-dependent carbamoyl phosphate synthase, cytidine triphosphate synthetase, gamma-glutamyl hydrolase, imidazole glycerol phosphate synthase and, cobyric acid synthase. Glutamine amidotransferase (GATase) domains can occur either as single polypeptides, as in glutamine amidotransferases, or as domains in a much larger multifunctional synthase protein, such as CPSase.


Pssm-ID: 153212 [Multi-domain]  Cd Length: 188  Bit Score: 189.76  E-value: 7.71e-61
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499349865   5 PFLIIETGHPVSGmkqyGRFPHWIRvAAGLAERETVVIDVANGDRLPDRRGFAGTLISGSAAFV-TDRADWSERSAEWLR 83
Cdd:cd01741    1 RILILQHDTPEGP----GLFEDLLR-EAGAETIEIDVVDVYAGELLPDLDDYDGLVILGGPMSVdEDDYPWLKKLKELIR 75

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499349865  84 DAAHAGMPLLGICYGHQLIAHALGGQVDYNPAGRESGTIALELHPPAHEDPLFAGLPPQFPAHATHLQTVLRAPDGAVVL 163
Cdd:cd01741   76 QALAAGKPVLGICLGHQLLARALGGKVGRNPKGWEIGWFPVTLTEAGKADPLFAGLPDEFPVFHWHGDTVVELPPGAVLL 155

                        170       180
                 ....*....|....*....|....*
gi 499349865 164 ARSPQDQCHAFRWGQSTWGVQFHPE 188
Cdd:cd01741  156 ASSEACPNQAFRYGDRALGLQFHPE 180
PRK07567 PRK07567
glutamine amidotransferase; Provisional
 31-237 9.93e-28

glutamine amidotransferase; Provisional


Pssm-ID: 181035 [Multi-domain]  Cd Length: 242  Bit Score: 106.18  E-value: 9.93e-28
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499349865  31 AAGLAERETVVIDVANGD-RLPDRRGFAGTLISGSAAFVTDRAD----WSERSAEWLRDAAH----AGMPLLGICYGHQL 101
Cdd:PRK07567  26 YTGLDPAELRRIRLDREPlPDLDLDDYSGVIVGGSPFNVSDPAEskspWQRRVEAELSGLLDevvaRDFPFLGACYGVGT 105

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499349865 102 IAHALGGQVDyNPAGRESGTIALELHPPAHEDPLFAGLPPQFPAHATHLQTVLRAPDGAVVLARSPQDQCHAFRWGQSTW 181
Cdd:PRK07567 106 LGHHQGGVVD-RTYGEPVGAVTVSLTDAGRADPLLAGLPDTFTAFVGHKEAVSALPPGAVLLATSPTCPVQMFRVGENVY 184

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 499349865 182 GVQFHPEFATHHMrgyvRARADCIARHGRC---------ARTVASEVSAAPmarKLLRRFVHHAR 237
Cdd:PRK07567 185 ATQFHPELDADGL----KTRIDFYRDHGYFapeeadsliARARSVDVTAPN---RILRNFVERYR 242
GATase1_GMP_Synthase cd01742
Type 1 glutamine amidotransferase (GATase1) domain found in GMP synthetase; Type 1 glutamine ...
 89-188 3.11e-27

Type 1 glutamine amidotransferase (GATase1) domain found in GMP synthetase; Type 1 glutamine amidotransferase (GATase1) domain found in GMP synthetase. GMP synthetase is a glutamine amidotransferase from the de novo purine biosynthetic pathway. Glutamine amidotransferase (GATase) activity catalyse the transfer of ammonia from the amide side chain of glutamine to an acceptor substrate. GMP synthetase catalyses the amination of the nucleotide precursor xanthosine 5'-monophosphate to form GMP. GMP synthetase belongs to the triad family of amidotransferases having a conserved Cys-His-Glu catalytic triad in the glutaminase active site.


Pssm-ID: 153213 [Multi-domain]  Cd Length: 181  Bit Score: 103.38  E-value: 3.11e-27
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499349865  89 GMPLLGICYGHQLIAHALGGQVDYNPaGRESGTIALELhppAHEDPLFAGLPPQFPAHATHLQTVLRAPDGAVVLARSPQ 168
Cdd:cd01742   70 GVPVLGICYGMQLIAKALGGKVERGD-KREYGKAEIEI---DDSSPLFEGLPDEQTVWMSHGDEVVKLPEGFKVIASSDN 145

                         90       100
                 ....*....|....*....|.
gi 499349865 169 DQCHAFR-WGQSTWGVQFHPE 188
Cdd:cd01742  146 CPVAAIAnEEKKIYGVQFHPE 166
guaA_Nterm TIGR00888
GMP synthase (glutamine-hydrolyzing), N-terminal domain or A subunit; This protein of purine ...
 57-188 7.19e-27

GMP synthase (glutamine-hydrolyzing), N-terminal domain or A subunit; This protein of purine de novo biosynthesis is well-conserved. However, it appears to split into two separate polypeptide chains in most of the Archaea. This N-terminal region would be the smaller subunit. [Purines, pyrimidines, nucleosides, and nucleotides, Purine ribonucleotide biosynthesis]


Pssm-ID: 129966 [Multi-domain]  Cd Length: 188  Bit Score: 102.39  E-value: 7.19e-27
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499349865   57 AGTLISGSAAFVtdradWSERSAEWLRDAAHAGMPLLGICYGHQLIAHALGGQVDYNPAgRESGTIALELhppAHEDPLF 136
Cdd:TIGR00888  43 KGIILSGGPSSV-----YAENAPRADEKIFELGVPVLGICYGMQLMAKQLGGEVGRAEK-REYGKAELEI---LDEDDLF 113

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|...
gi 499349865  137 AGLPPQFPAHATHLQTVLRAPDGAVVLARSPQDQCHAFR-WGQSTWGVQFHPE 188
Cdd:TIGR00888 114 RGLPDESTVWMSHGDKVKELPEGFKVLATSDNCPVAAMAhEEKPIYGVQFHPE 166
guaA PRK00074
GMP synthase; Reviewed
 88-235 2.73e-21

GMP synthase; Reviewed


Pssm-ID: 234614 [Multi-domain]  Cd Length: 511  Bit Score: 92.42  E-value: 2.73e-21
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499349865  88 AGMPLLGICYGHQLIAHALGGQVDynPAG-RESGTIALELHppaHEDPLFAGLPPQFPAHATHLQTVLRAPDGAVVLARS 166
Cdd:PRK00074  74 LGVPVLGICYGMQLMAHQLGGKVE--RAGkREYGRAELEVD---NDSPLFKGLPEEQDVWMSHGDKVTELPEGFKVIAST 148

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499349865 167 PQDQCHAFRW-GQSTWGVQFHPEfATHHMRGyvraradciarhgrcartvasevsaapmaRKLLRRFVHH 235
Cdd:PRK00074 149 ENCPIAAIANeERKFYGVQFHPE-VTHTPQG-----------------------------KKLLENFVFD 188
PRK00758 PRK00758
GMP synthase subunit A; Validated
 77-190 1.48e-20

GMP synthase subunit A; Validated


Pssm-ID: 179112 [Multi-domain]  Cd Length: 184  Bit Score: 85.67  E-value: 1.48e-20
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499349865  77 RSAEWLRDAahaGMPLLGICYGHQLIAHALGGQVDYNPAGrESGTIALELhppAHEDPLFAGLPPQFPAHATHLQTVLRA 156
Cdd:PRK00758  58 NCPEYLKEL---DVPILGICLGHQLIAKAFGGEVGRGEYG-EYALVEVEI---LDEDDILKGLPPEIRVWASHADEVKEL 130

                         90       100       110
                 ....*....|....*....|....*....|....*
gi 499349865 157 PDGAVVLARSPQDQCHAFRWG-QSTWGVQFHPEFA 190
Cdd:PRK00758 131 PDGFEILARSDICEVEAMKHKeKPIYGVQFHPEVA 165
PRK06490 PRK06490
glutamine amidotransferase; Provisional
 47-194 1.67e-16

glutamine amidotransferase; Provisional


Pssm-ID: 180590 [Multi-domain]  Cd Length: 239  Bit Score: 76.15  E-value: 1.67e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499349865  47 GDRLPDR-RGFAGTLISGSAAFVTDRADWSERSAEWLRDAAHAGMPLLGICYGHQLIAHALGGQVDYNPAGR-ESGTiaL 124
Cdd:PRK06490  43 GDPLPDTlEDHAGAVIFGGPMSANDPDDFIRREIDWISVPLKENKPFLGICLGAQMLARHLGARVAPHPDGRvEIGY--Y 120

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 499349865 125 ELHPPAHEDPLfaglpPQFPAHATHLQTV-LRAPDGAVVLARSPQDQCHAFRWGQSTWGVQFHPEFaTHHM 194
Cdd:PRK06490 121 PLRPTEAGRAL-----MHWPEMVYHWHREgFDLPAGAELLATGDDFPNQAFRYGDNAWGLQFHPEV-TRAM 185
PRK05665 PRK05665
amidotransferase; Provisional
 21-235 5.61e-15

amidotransferase; Provisional


Pssm-ID: 168162 [Multi-domain]  Cd Length: 240  Bit Score: 72.15  E-value: 5.61e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499349865  21 YGRFPHWIRVAAGLAErETVVIDVANGDRLPDRRGFAGTLISGSAA--FVTDraDWSERSAEWLRDAAHAGMPLLGICYG 98
Cdd:PRK05665  24 YGRMFEQLFARQPIAA-EFVVYNVVQGDYPADDEKFDAYLVTGSKAdsFGTD--PWIQTLKTYLLKLYERGDKLLGVCFG 100

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499349865  99 HQLIAHALGGQVDYNPAGRESGTIALELHPPAhedPLFAGLPPQFPAHATHLQTVLRAPDGAVVLARSPQDQCHAFRWGQ 178
Cdd:PRK05665 101 HQLLALLLGGKAERASQGWGVGIHRYQLAAHA---PWMSPAVTELTLLISHQDQVTALPEGATVIASSDFCPFAAYHIGD 177

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*....
gi 499349865 179 STWGVQFHPEFATHHMRGYVRARADCI--ARHGRCARTVASEVSAAPMARKLLrRFVHH 235
Cdd:PRK05665 178 QVLCFQGHPEFVHDYSRALLDLRQEHLgeEVYSKGVASLAHDHQGTTVAEWMM-RFVAQ 235
PRK07053 PRK07053
glutamine amidotransferase; Provisional
 66-214 1.10e-14

glutamine amidotransferase; Provisional


Pssm-ID: 235919 [Multi-domain]  Cd Length: 234  Bit Score: 71.13  E-value: 1.10e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499349865  66 AFVTDRADWSERSAEWLRDAAHAGMPLLGICYGHQLIAHALGGQVdYNPAGRESGTIALELHPPAHEDPLfAGLPPQFPA 145
Cdd:PRK07053  60 VYDDELYPFLAPEIALLRQRLAAGLPTLGICLGAQLIARALGARV-YPGGQKEIGWAPLTLTDAGRASPL-RHLGAGTPV 137

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 499349865 146 HATHLQTvLRAPDGAVVLARSPQDQCHAFRWGQSTWGVQFHPEFATHHMRGYVRARADCIARHGRCART 214
Cdd:PRK07053 138 LHWHGDT-FDLPEGATLLASTPACRHQAFAWGNHVLALQFHPEAREDRFEAWLIGHAGELAAAGIDPRT 205
PabA COG0512
Anthranilate/para-aminobenzoate synthase component II (glutamine amidotransferase) [Amino acid ...
 78-188 2.75e-14

Anthranilate/para-aminobenzoate synthase component II (glutamine amidotransferase) [Amino acid transport and metabolism, Coenzyme transport and metabolism]; Anthranilate/para-aminobenzoate synthase component II (glutamine amidotransferase) is part of the Pathway/BioSystem: Aromatic amino acid biosynthesis


Pssm-ID: 440278 [Multi-domain]  Cd Length: 189  Bit Score: 68.91  E-value: 2.75e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499349865  78 SAEWLRdAAHAGMPLLGICYGHQLIAHALGGQVDynPAGResgtialelhpPAH---------EDPLFAGLPPQFPahAT 148
Cdd:COG0512   61 SLEVIR-AFAGKIPILGVCLGHQAIGEAFGGKVV--RAPE-----------PMHgktspithdGSGLFAGLPNPFT--AT 124

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*....
gi 499349865 149 --HLQTVLRA--PDGAVVLARSPQDQCHAFR-----WgqstWGVQFHPE 188
Cdd:COG0512  125 ryHSLVVDREtlPDELEVTAWTEDGEIMGIRhrelpI----EGVQFHPE 169
GATase1_Anthranilate_Synthase cd01743
Type 1 glutamine amidotransferase (GATase1) domain found in Anthranilate synthase; Type 1 ...
 91-193 5.16e-14

Type 1 glutamine amidotransferase (GATase1) domain found in Anthranilate synthase; Type 1 glutamine amidotransferase (GATase1) domain found in Anthranilate synthase (ASase). This group contains proteins similar to para-aminobenzoate (PABA) synthase and ASase. These enzymes catalyze similar reactions and produce similar products, PABA and ortho-aminobenzoate (anthranilate). Each enzyme is composed of non-identical subunits: a glutamine amidotransferase subunit (component II) and a subunit that produces an aminobenzoate products (component I). ASase catalyses the synthesis of anthranilate from chorismate and glutamine and is a tetrameric protein comprising two copies each of components I and II. Component II of ASase belongs to the family of triad GTases which hydrolyze glutamine and transfer nascent ammonia between the active sites. In some bacteria, such as Escherichia coli, component II can be much larger than in other organisms, due to the presence of phosphoribosyl-anthranilate transferase (PRTase) activity. PRTase catalyses the second step in tryptophan biosynthesis and results in the addition of 5-phosphoribosyl-1-pyrophosphate to anthranilate to create N-5'-phosphoribosyl-anthranilate. In E.coli, the first step in the conversion of chorismate to PABA involves two proteins: PabA and PabB which co-operate to transfer the amide nitrogen of glutamine to chorismate forming 4-amino-4 deoxychorismate (ADC). PabA acts as a glutamine amidotransferase, supplying an amino group to PabB, which carries out the amination reaction. A third protein PabC then mediates elimination of pyruvate and aromatization to give PABA. Several organisms have bipartite proteins containing fused domains homologous to PabA and PabB commonly called PABA synthases. These hybrid PABA synthases may produce ADC and not PABA.


Pssm-ID: 153214 [Multi-domain]  Cd Length: 184  Bit Score: 68.33  E-value: 5.16e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499349865  91 PLLGICYGHQLIAHALGGQVDYnpagresgtialeLHPPAH---------EDPLFAGLPPQFPA------HATHlqtvLR 155
Cdd:cd01743   73 PILGVCLGHQAIAEAFGGKVVR-------------APEPMHgktseihhdGSGLFKGLPQPFTVgryhslVVDP----DP 135

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|
gi 499349865 156 APDGAVVLARSPQDQCHAFRWGQST-WGVQFHPE-FATHH 193
Cdd:cd01743  136 LPDLLEVTASTEDGVIMALRHRDLPiYGVQFHPEsILTEY 175
GATase pfam00117
Glutamine amidotransferase class-I;
82-189 4.10e-13

Glutamine amidotransferase class-I;


Pssm-ID: 395067 [Multi-domain]  Cd Length: 188  Bit Score: 65.72  E-value: 4.10e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499349865   82 LRDAAHAGMPLLGICYGHQLIAHALGGQVDynPAGRES---GTIALELHPPAhedpLFAGLPPQFPAHATHLQTV--LRA 156
Cdd:pfam00117  63 IREARELKIPILGICLGHQLLALAFGGKVV--KAKKFGhhgKNSPVGDDGCG----LFYGLPNVFIVRRYHSYAVdpDTL 136

                          90       100       110
                  ....*....|....*....|....*....|....*
gi 499349865  157 PDGAVVLARSPQDQC-HAFRWGQSTW-GVQFHPEF 189
Cdd:pfam00117 137 PDGLEVTATSENDGTiMGIRHKKLPIfGVQFHPES 171
PRK05670 PRK05670
anthranilate synthase component II; Provisional
 91-188 2.98e-12

anthranilate synthase component II; Provisional


Pssm-ID: 235552 [Multi-domain]  Cd Length: 189  Bit Score: 63.61  E-value: 2.98e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499349865  91 PLLGICYGHQLIAHALGGQVdynpagRESGTIaleLH----PPAHED-PLFAGLPPQFPAHATHLQTVLRA--PDGAVVL 163
Cdd:PRK05670  74 PILGVCLGHQAIGEAFGGKV------VRAKEI---MHgktsPIEHDGsGIFAGLPNPFTVTRYHSLVVDREslPDCLEVT 144

                         90       100
                 ....*....|....*....|....*.
gi 499349865 164 ARSPQDQCHAFRWGQ-STWGVQFHPE 188
Cdd:PRK05670 145 AWTDDGEIMGVRHKElPIYGVQFHPE 170
PLN02347 PLN02347
GMP synthetase
 85-196 1.09e-11

GMP synthetase


Pssm-ID: 215197 [Multi-domain]  Cd Length: 536  Bit Score: 64.32  E-value: 1.09e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499349865  85 AAHAGMPLLGICYGHQLIAHALGGQVDynPA-GRESGTIALElhpPAHEDPLFAGLP--PQFPAHATHLQTVLRAPDGAV 161
Cdd:PLN02347  82 CRERGVPVLGICYGMQLIVQKLGGEVK--PGeKQEYGRMEIR---VVCGSQLFGDLPsgETQTVWMSHGDEAVKLPEGFE 156

                         90       100       110
                 ....*....|....*....|....*....|....*.
gi 499349865 162 VLARSPQDQCHAFRWGQST-WGVQFHPEfATHHMRG 196
Cdd:PLN02347 157 VVAKSVQGAVVAIENRERRiYGLQYHPE-VTHSPKG 191
PRK07765 PRK07765
aminodeoxychorismate/anthranilate synthase component II;
83-188 8.77e-11

aminodeoxychorismate/anthranilate synthase component II;


Pssm-ID: 181107 [Multi-domain]  Cd Length: 214  Bit Score: 59.68  E-value: 8.77e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499349865  83 RDAAHAGMPLLGICYGHQLIAHALGGQVDYNPA---GRESgtialELHppaHEDP-LFAGLPPQFPAHATHLQTVLRA-- 156
Cdd:PRK07765  70 RACAAAGTPLLGVCLGHQAIGVAFGATVDRAPEllhGKTS-----SVH---HTGVgVLAGLPDPFTATRYHSLTILPEtl 141

                         90       100       110
                 ....*....|....*....|....*....|...
gi 499349865 157 PDGAVVLARSPQDQCHAFRWGQ-STWGVQFHPE 188
Cdd:PRK07765 142 PAELEVTARTDSGVIMAVRHRElPIHGVQFHPE 174
PLN02335 PLN02335
anthranilate synthase
 91-188 1.08e-09

anthranilate synthase


Pssm-ID: 177969 [Multi-domain]  Cd Length: 222  Bit Score: 56.73  E-value: 1.08e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499349865  91 PLLGICYGHQLIAHALGGQVDYNPAGRESGTIALELHPPAHEDPLFAGLPPQFPAHATH-------------LQTVLRAP 157
Cdd:PLN02335  93 PLFGVCMGLQCIGEAFGGKIVRSPFGVMHGKSSPVHYDEKGEEGLFSGLPNPFTAGRYHslviekdtfpsdeLEVTAWTE 172

                         90       100       110
                 ....*....|....*....|....*....|.
gi 499349865 158 DGAVVLARSpqdqcHAFRWGQstwGVQFHPE 188
Cdd:PLN02335 173 DGLIMAARH-----RKYKHIQ---GVQFHPE 195
PuuD COG2071
Gamma-glutamyl-gamma-aminobutyrate hydrolase PuuD (putrescine degradation), contains ...
 80-193 4.15e-08

Gamma-glutamyl-gamma-aminobutyrate hydrolase PuuD (putrescine degradation), contains GATase1-like domain [Amino acid transport and metabolism];


Pssm-ID: 441674 [Multi-domain]  Cd Length: 231  Bit Score: 52.48  E-value: 4.15e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499349865  80 EWLRDAAHAGMPLLGICYGHQLIAHALGG--------QVD-----YNPAGRESGTIALELHPpaheDPLFAGL--PPQFP 144
Cdd:COG2071   87 ALIRAALERGKPVLGICRGMQLLNVALGGtlyqdlpdQVPgaldhRQPAPRYAPRHTVEIEP----GSRLARIlgEEEIR 162

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*.
gi 499349865 145 AHATHLQTVLRAPDGAVVLARSP-------QDQCHAFrwgqsTWGVQFHPEFATHH 193
Cdd:COG2071  163 VNSLHHQAVKRLGPGLRVSARAPdgvieaiESPGAPF-----VLGVQWHPEWLAAS 213
Peptidase_C26 pfam07722
Peptidase C26; These peptidases have gamma-glutamyl hydrolase activity; that is they catalyze ...
 82-188 8.69e-08

Peptidase C26; These peptidases have gamma-glutamyl hydrolase activity; that is they catalyze the cleavage of the gamma-glutamyl bond in poly-gamma-glutamyl substrates. They are structurally related to pfam00117, but contain extensions in four loops and at the C terminus.


Pssm-ID: 429620 [Multi-domain]  Cd Length: 219  Bit Score: 51.10  E-value: 8.69e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499349865   82 LRDAAHAGMPLLGICYGHQLIAHALGG-------QVDYNPAGRESGTIALELhpPAH-----EDPLFAGLPP--QFPAHA 147
Cdd:pfam07722  98 IRAALARGKPILGICRGFQLLNVALGGtlyqdiqEQPGFTDHREHCQVAPYA--PSHavnvePGSLLASLLGseEFRVNS 175

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....
gi 499349865  148 THLQTVLRAPDGAVVLARSPQDQCHAFRWGQSTW---GVQFHPE 188
Cdd:pfam07722 176 LHHQAIDRLAPGLRVEAVAPDGTIEAIESPNAKGfalGVQWHPE 219
GATase1_2 cd01745
Subgroup of proteins having the Type 1 glutamine amidotransferase (GATase1) domain; This group ...
 69-189 2.11e-07

Subgroup of proteins having the Type 1 glutamine amidotransferase (GATase1) domain; This group contains a subgroup of proteins having the Type 1 glutamine amidotransferase (GATase1) domain. GATase activity catalyses the transfer of ammonia from the amide side chain of glutamine to an acceptor substrate. Glutamine amidotransferases (GATase) includes the triad family of amidotransferases which have a conserved Cys-His-Glu catalytic triad in the glutaminase active site. In this subgroup this triad is conserved. GATase activity can be found in a range of biosynthetic enzymes, including: glutamine amidotransferase, formylglycinamide ribonucleotide, GMP synthetase , anthranilate synthase component II, glutamine-dependent carbamoyl phosphate synthase, cytidine triphosphate synthetase, gamma-glutamyl hydrolase, imidazole glycerol phosphate synthase and, cobyric acid synthase. Glutamine amidotransferase (GATase) domains can occur either as single polypeptides, as in glutamine amidotransferases, or as domains in a much larger multifunctional synthase protein, such as CPSase.


Pssm-ID: 153216 [Multi-domain]  Cd Length: 189  Bit Score: 49.88  E-value: 2.11e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499349865  69 TDRA-DWSERsaEWLRDAAHAGMPLLGICYGHQLIAHALGGqvdynpagresgtialELHPpahedplfaglppqfpaHA 147
Cdd:cd01745   81 IDPErDAFEL--ALLRAALERGKPILGICRGMQLLNVALGG----------------TLYQ-----------------DI 125

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*...
gi 499349865 148 T----HLQTVLRAPDGAVVLARSPQDQCHAFRWGQSTW--GVQFHPEF 189
Cdd:cd01745  126 RvnslHHQAIKRLADGLRVEARAPDGVIEAIESPDRPFvlGVQWHPEW 173
trpG CHL00101
anthranilate synthase component 2
 91-188 3.08e-07

anthranilate synthase component 2


Pssm-ID: 214365 [Multi-domain]  Cd Length: 190  Bit Score: 49.34  E-value: 3.08e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499349865  91 PLLGICYGHQLIAHALGGQVDYNPAGREsGTIALELHppAHEDpLFAGLPPQFPAHATHLQTVLRA--PDGAVVLARSPQ 168
Cdd:CHL00101  74 PILGVCLGHQSIGYLFGGKIIKAPKPMH-GKTSKIYH--NHDD-LFQGLPNPFTATRYHSLIIDPLnlPSPLEITAWTED 149

                         90       100
                 ....*....|....*....|..
gi 499349865 169 DQCHAFR--WGQSTWGVQFHPE 188
Cdd:CHL00101 150 GLIMACRhkKYKMLRGIQFHPE 171
PRK14607 PRK14607
bifunctional anthranilate synthase component II/anthranilate phosphoribosyltransferase;
90-188 5.32e-07

bifunctional anthranilate synthase component II/anthranilate phosphoribosyltransferase;


Pssm-ID: 237764 [Multi-domain]  Cd Length: 534  Bit Score: 50.10  E-value: 5.32e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499349865  90 MPLLGICYGHQLIAHALGGQVDYNPA---GRESgtialelhpPAHEDP--LFAGLPPQFPAHATHLQTVLRA--PDGAVV 162
Cdd:PRK14607  74 VPILGVCLGHQAIGYAFGGKIVHAKRilhGKTS---------PIDHNGkgLFRGIPNPTVATRYHSLVVEEAslPECLEV 144

                         90       100
                 ....*....|....*....|....*..
gi 499349865 163 LARSPQDQCHAFRWGQ-STWGVQFHPE 188
Cdd:PRK14607 145 TAKSDDGEIMGIRHKEhPIFGVQFHPE 171
PRK07649 PRK07649
aminodeoxychorismate/anthranilate synthase component II;
90-188 2.58e-06

aminodeoxychorismate/anthranilate synthase component II;


Pssm-ID: 181066 [Multi-domain]  Cd Length: 195  Bit Score: 46.72  E-value: 2.58e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499349865  90 MPLLGICYGHQLIAHALGGQVDYNPAGRESGTIALElhppaHE-DPLFAGLPPQFPAHATHLQTVLRA--PDGAVVLARS 166
Cdd:PRK07649  73 IPIFGVCLGHQSIAQVFGGEVVRAERLMHGKTSLMH-----HDgKTIFSDIPNPFTATRYHSLIVKKEtlPDCLEVTSWT 147

                         90       100
                 ....*....|....*....|...
gi 499349865 167 PQDQCHAFRWGQ-STWGVQFHPE 188
Cdd:PRK07649 148 EEGEIMAIRHKTlPIEGVQFHPE 170
GATase1 cd01653
Type 1 glutamine amidotransferase (GATase1)-like domain; Type 1 glutamine amidotransferase ...
 38-108 3.16e-06

Type 1 glutamine amidotransferase (GATase1)-like domain; Type 1 glutamine amidotransferase (GATase1)-like domain. This group includes proteins similar to Class I glutamine amidotransferases, the intracellular PH1704 from Pyrococcus horikoshii, the C-terminal of the large catalase: Escherichia coli HP-II, Sinorhizobium meliloti Rm1021 ThuA. and, the A4 beta-galactosidase middle domain. The majority of proteins in this group have a reactive Cys found in the sharp turn between a beta strand and an alpha helix termed the nucleophile elbow. For Class I glutamine amidotransferases proteins which transfer ammonia from the amide side chain of glutamine to an acceptor substrate, this Cys forms a Cys-His-Glu catalytic triad in the active site. Glutamine amidotransferases activity can be found in a range of biosynthetic enzymes included in this cd: glutamine amidotransferase, formylglycinamide ribonucleotide, GMP synthetase, anthranilate synthase component II, glutamine-dependent carbamoyl phosphate synthase, cytidine triphosphate synthetase, gamma-glutamyl hydrolase, imidazole glycerol phosphate synthase and, cobyric acid synthase. For Pyrococcus horikoshii PH1704, the Cys of the nucleophile elbow together with a different His and, a Glu from an adjacent monomer form a catalytic triad different from the typical GATase1 triad. The E. coli HP-II C-terminal domain, S. meliloti Rm1021 ThuA and the A4 beta-galactosidase middle domain lack the catalytic triad typical GATaseI domains. GATase1-like domains can occur either as single polypeptides, as in Class I glutamine amidotransferases, or as domains in a much larger multifunctional synthase protein, such as CPSase.


Pssm-ID: 153210 [Multi-domain]  Cd Length: 115  Bit Score: 44.90  E-value: 3.16e-06
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 499349865  38 ETVVIDVANGDRLPDRR--GFAGTLISGSAAFVTDRAdWSERSAEWLRDAAHAGMPLLGICYGHQLIAHALGG 108
Cdd:cd01653   27 EVDVVSPDGGPVESDVDldDYDGLILPGGPGTPDDLA-RDEALLALLREAAAAGKPILGICLGAQLLVLGVQF 98
PRK13566 PRK13566
anthranilate synthase component I;
84-188 5.82e-06

anthranilate synthase component I;


Pssm-ID: 237429 [Multi-domain]  Cd Length: 720  Bit Score: 46.83  E-value: 5.82e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499349865  84 DAAHA-GMPLLGICYGHQLIAHALGGQVDY--NPAGRESGTIALElhppaHEDPLFAGLPPQFPAHATHLQTVLRA--PD 158
Cdd:PRK13566 592 DAALArNLPIFGVCLGLQAIVEAFGGELGQlaYPMHGKPSRIRVR-----GPGRLFSGLPEEFTVGRYHSLFADPEtlPD 666

                         90       100       110
                 ....*....|....*....|....*....|...
gi 499349865 159 GAVVLARSPQDQCHAFRwgQST---WGVQFHPE 188
Cdd:PRK13566 667 ELLVTAETEDGVIMAIE--HKTlpvAAVQFHPE 697
GAT_1 cd03128
Type 1 glutamine amidotransferase (GATase1)-like domain; Type 1 glutamine amidotransferase ...
 38-102 7.43e-06

Type 1 glutamine amidotransferase (GATase1)-like domain; Type 1 glutamine amidotransferase (GATase1)-like domain. This group contains proteins similar to Class I glutamine amidotransferases, the intracellular PH1704 from Pyrococcus horikoshii, the C-terminal of the large catalase: Escherichia coli HP-II, Sinorhizobium meliloti Rm1021 ThuA, the A4 beta-galactosidase middle domain and peptidase E. The majority of proteins in this group have a reactive Cys found in the sharp turn between a beta strand and an alpha helix termed the nucleophile elbow. For Class I glutamine amidotransferases proteins which transfer ammonia from the amide side chain of glutamine to an acceptor substrate, this Cys forms a Cys-His-Glu catalytic triad in the active site. Glutamine amidotransferases activity can be found in a range of biosynthetic enzymes included in this cd: glutamine amidotransferase, formylglycinamide ribonucleotide, GMP synthetase, anthranilate synthase component II, glutamine-dependent carbamoyl phosphate synthase (CPSase), cytidine triphosphate synthetase, gamma-glutamyl hydrolase, imidazole glycerol phosphate synthase and, cobyric acid synthase. For Pyrococcus horikoshii PH1704, the Cys of the nucleophile elbow together with a different His and, a Glu from an adjacent monomer form a catalytic triad different from the typical GATase1 triad. Peptidase E is believed to be a serine peptidase having a Ser-His-Glu catalytic triad which differs from the Cys-His-Glu catalytic triad of typical GATase1 domains, by having a Ser in place of the reactive Cys at the nucleophile elbow. The E. coli HP-II C-terminal domain, S. meliloti Rm1021 ThuA and the A4 beta-galactosidase middle domain lack the catalytic triad typical GATaseI domains. GATase1-like domains can occur either as single polypeptides, as in Class I glutamine amidotransferases, or as domains in a much larger multifunctional synthase protein, such as CPSase. Peptidase E has a circular permutation in the common core of a typical GTAse1 domain.


Pssm-ID: 153222 [Multi-domain]  Cd Length: 92  Bit Score: 43.34  E-value: 7.43e-06
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 499349865  38 ETVVIDVANGD--RLPDRRGFAGTLISGSAAFVTDRAdWSERSAEWLRDAAHAGMPLLGICYGHQLI 102
Cdd:cd03128   27 EVDVVSPDGGPveSDVDLDDYDGLILPGGPGTPDDLA-WDEALLALLREAAAAGKPVLGICLGAQLL 92
CarA COG0505
Carbamoylphosphate synthase small subunit [Amino acid transport and metabolism, Nucleotide ...
 82-108 1.21e-05

Carbamoylphosphate synthase small subunit [Amino acid transport and metabolism, Nucleotide transport and metabolism]; Carbamoylphosphate synthase small subunit is part of the Pathway/BioSystem: Arginine biosynthesis


Pssm-ID: 440271 [Multi-domain]  Cd Length: 361  Bit Score: 45.78  E-value: 1.21e-05
                         10        20
                 ....*....|....*....|....*..
gi 499349865  82 LRDAAHAGMPLLGICYGHQLIAHALGG 108
Cdd:COG0505  240 IRELLGKGIPIFGICLGHQLLALALGA 266
PRK12564 PRK12564
carbamoyl-phosphate synthase small subunit;
82-109 1.91e-05

carbamoyl-phosphate synthase small subunit;


Pssm-ID: 237139 [Multi-domain]  Cd Length: 360  Bit Score: 45.07  E-value: 1.91e-05
                         10        20
                 ....*....|....*....|....*...
gi 499349865  82 LRDAAHAGMPLLGICYGHQLIAHALGGQ 109
Cdd:PRK12564 241 IRELLEKKIPIFGICLGHQLLALALGAK 268
GATase1_CPSase cd01744
Small chain of the glutamine-dependent form of carbamoyl phosphate synthase, CPSase II; This ...
 82-109 1.96e-05

Small chain of the glutamine-dependent form of carbamoyl phosphate synthase, CPSase II; This group of sequences represents the small chain of the glutamine-dependent form of carbamoyl phosphate synthase, CPSase II. CPSase II catalyzes the production of carbomyl phosphate (CP) from bicarbonate, glutamine and two molecules of MgATP. The reaction is believed to proceed by a series of four biochemical reactions involving a minimum of three discrete highly reactive intermediates. The synthesis of CP is critical for the initiation of two separate biosynthetic pathways. In one CP is coupled to aspartate, its carbon and nitrogen nuclei ultimately incorporated into the aromatic moieties of pyrimidine nucleotides. In the second pathway CP is condensed with ornithine at the start of the urea cycle and is utilized for the detoxification of ammonia and biosynthesis of arginine. CPSases may be encoded by one or by several genes, depending on the species. The E.coli enzyme is a heterodimer consisting of two polypeptide chains referred to as the small and large subunit. Ammonia an intermediate during the biosynthesis of carbomyl phosphate produced by the hydrolysis of glutamine in the small subunit of the enzyme is delivered via a molecular tunnel between the remotely located carboxyphosphate active site in the large subunit. CPSase IIs belong to the triad family of amidotransferases having a conserved Cys-His-Glu catalytic triad in the glutaminase active site. This group also contains the sequence from the mammalian urea cycle form which has lost the active site Cys, resulting in an ammonia-dependent form, CPSase I.


Pssm-ID: 153215 [Multi-domain]  Cd Length: 178  Bit Score: 44.02  E-value: 1.96e-05
                         10        20
                 ....*....|....*....|....*...
gi 499349865  82 LRDAAHAGMPLLGICYGHQLIAHALGGQ 109
Cdd:cd01744   62 VRKLLGKKIPIFGICLGHQLLALALGAK 89
PRK06895 PRK06895
anthranilate synthase component II;
92-193 2.75e-05

anthranilate synthase component II;


Pssm-ID: 235882 [Multi-domain]  Cd Length: 190  Bit Score: 43.57  E-value: 2.75e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499349865  92 LLGICYGHQLIAHALGGQVdYN-PAGRESGTIALELHPPaheDPLFAGLPPQFPAHATHLQTVLRA--PDGAVVLARSPQ 168
Cdd:PRK06895  75 ILGVCLGHQTLCEFFGGEL-YNlNNVRHGQQRPLKVRSN---SPLFDGLPEEFNIGLYHSWAVSEEnfPTPLEITAVCDE 150

                         90       100
                 ....*....|....*....|....*..
gi 499349865 169 DQCHAFRWGQ-STWGVQFHPE-FATHH 193
Cdd:PRK06895 151 NVVMAMQHKTlPIYGVQFHPEsYISEF 177
trpG_papA TIGR00566
glutamine amidotransferase of anthranilate synthase or aminodeoxychorismate synthase; This ...
 90-188 2.84e-05

glutamine amidotransferase of anthranilate synthase or aminodeoxychorismate synthase; This model describes the glutamine amidotransferase domain or peptide of the tryptophan-biosynthetic pathway enzyme anthranilate synthase or of the folate biosynthetic pathway enzyme para-aminobenzoate synthase. In at least one case, a single polypeptide from Bacillus subtilis was shown to have both functions. This model covers a subset of the sequences described by the Pfam model GATase.


Pssm-ID: 273144 [Multi-domain]  Cd Length: 188  Bit Score: 43.62  E-value: 2.84e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499349865   90 MPLLGICYGHQLIAHALGGQVDYNPAGRESGTIALELHPPAhedpLFAGLPPQFPA---HATHLQTVlRAPDGAVVLARS 166
Cdd:TIGR00566  73 LPILGVCLGHQAMGQAFGGDVVRANTVMHGKTSEIEHNGAG----IFRGLFNPLTAtryHSLVVEPE-TLPTCFPVTAWE 147

                          90       100
                  ....*....|....*....|....
gi 499349865  167 PQDQ-CHAFRWGQSTW-GVQFHPE 188
Cdd:TIGR00566 148 EENIeIMAIRHRDLPLeGVQFHPE 171
PRK09522 PRK09522
bifunctional anthranilate synthase glutamate amidotransferase component TrpG/anthranilate ...
 90-188 3.92e-05

bifunctional anthranilate synthase glutamate amidotransferase component TrpG/anthranilate phosphoribosyltransferase TrpD;


Pssm-ID: 181927 [Multi-domain]  Cd Length: 531  Bit Score: 44.25  E-value: 3.92e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499349865  90 MPLLGICYGHQLIAHALGGQVDynpagrESGTIaleLHPPA----HE-DPLFAGLPPQFPAHATHLQTVLRAPDGAVVLA 164
Cdd:PRK09522  78 LPIIGICLGHQAIVEAYGGYVG------QAGEI---LHGKAssieHDgQAMFAGLTNPLPVARYHSLVGSNIPAGLTINA 148

                         90       100
                 ....*....|....*....|....*
gi 499349865 165 rSPQDQCHAFRW-GQSTWGVQFHPE 188
Cdd:PRK09522 149 -HFNGMVMAVRHdADRVCGFQFHPE 172
PRK05637 PRK05637
anthranilate synthase component II; Provisional
 82-188 1.44e-04

anthranilate synthase component II; Provisional


Pssm-ID: 180178 [Multi-domain]  Cd Length: 208  Bit Score: 41.75  E-value: 1.44e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499349865  82 LRDAAHAGMPLLGICYGHQLIAHALGGQVDynPAGRESG-TIALELHPPAHEDPLFAGLP-------PQFPAHAT----- 148
Cdd:PRK05637  66 LIDRTLGQIPLLGICLGFQALLEHHGGKVE--PCGPVHGtTDNMILTDAGVQSPVFAGLAtdvepdhPEIPGRKVpiary 143

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....
gi 499349865 149 HLQTVLRAPDGAVVLARSPQDQCHAFRWGQST----WGVQFHPE 188
Cdd:PRK05637 144 HSLGCVVAPDGMESLGTCSSEIGPVIMAAETTdgkaIGLQFHPE 187
PRK08250 PRK08250
glutamine amidotransferase; Provisional
 83-189 5.48e-04

glutamine amidotransferase; Provisional


Pssm-ID: 181323 [Multi-domain]  Cd Length: 235  Bit Score: 40.34  E-value: 5.48e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499349865  83 RDAAHAGMPLLGICYGHQLIAHALGGQVDYNPAgRESGTIALELHPPAHEDPLFA----------------GLPPQfpah 146
Cdd:PRK08250  78 NQAIKAGKAVIGVCLGAQLIGEALGAKYEHSPE-KEIGYFPITLTEAGLKDPLLShfgstltvghwhndmpGLTDQ---- 152

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*
gi 499349865 147 athlqtvlrapdgAVVLARSpqDQC--HAFRWGQSTWGVQFHPEF 189
Cdd:PRK08250 153 -------------AKVLATS--EGCprQIVQYSNLVYGFQCHMEF 182
HisH COG0118
Imidazoleglycerol phosphate synthase glutamine amidotransferase subunit HisH [Amino acid ...
 80-188 6.73e-04

Imidazoleglycerol phosphate synthase glutamine amidotransferase subunit HisH [Amino acid transport and metabolism]; Imidazoleglycerol phosphate synthase glutamine amidotransferase subunit HisH is part of the Pathway/BioSystem: Histidine biosynthesis


Pssm-ID: 439888 [Multi-domain]  Cd Length: 196  Bit Score: 39.64  E-value: 6.73e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499349865  80 EWLRDAAHAGMPLLGICYGHQLIAHalggqvdynpAGRESGTIA-LEL----------------HP------PAHEDPLF 136
Cdd:COG0118   64 EAIREAVAGGKPVLGICLGMQLLFE----------RSEENGDTEgLGLipgevvrfpasdlkvpHMgwntveIAKDHPLF 133

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*...
gi 499349865 137 AGLPPQ----FpAHATHLQTvlraPDGAVVLARS--PQDQCHAFRWGqSTWGVQFHPE 188
Cdd:COG0118  134 AGIPDGeyfyF-VHSYYVPP----DDPEDVVATTdyGVPFTAAVERG-NVFGTQFHPE 185
CPSaseIIsmall TIGR01368
carbamoyl-phosphate synthase, small subunit; This model represents the whole of the small ...
 91-109 7.13e-04

carbamoyl-phosphate synthase, small subunit; This model represents the whole of the small chain of the glutamine-dependent form (EC 6.3.5.5) of carbamoyl phosphate synthase, CPSase II. The C-terminal domain has glutamine amidotransferase activity. Note that the sequence from the mammalian urea cycle form has lost the active site Cys, resulting in an ammonia-dependent form, CPSase I (EC 6.3.4.16). CPSases of pyrimidine biosynthesis, arginine biosynthesis, and the urea cycle may be encoded by one or by several genes, depending on the species. [Purines, pyrimidines, nucleosides, and nucleotides, Pyrimidine ribonucleotide biosynthesis]


Pssm-ID: 273580 [Multi-domain]  Cd Length: 357  Bit Score: 40.30  E-value: 7.13e-04
                          10
                  ....*....|....*....
gi 499349865   91 PLLGICYGHQLIAHALGGQ 109
Cdd:TIGR01368 244 PIFGICLGHQLLALAFGAK 262
PRK12838 PRK12838
carbamoyl phosphate synthase small subunit; Reviewed
 89-109 8.14e-04

carbamoyl phosphate synthase small subunit; Reviewed


Pssm-ID: 183784 [Multi-domain]  Cd Length: 354  Bit Score: 40.26  E-value: 8.14e-04
                         10        20
                 ....*....|....*....|.
gi 499349865  89 GMPLLGICYGHQLIAHALGGQ 109
Cdd:PRK12838 237 SYPILGICLGHQLIALALGAD 257
PRK08007 PRK08007
aminodeoxychorismate synthase component 2;
90-188 9.55e-04

aminodeoxychorismate synthase component 2;


Pssm-ID: 181194 [Multi-domain]  Cd Length: 187  Bit Score: 39.13  E-value: 9.55e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499349865  90 MPLLGICYGHQLIAHALGGQVdynpaGRESGTIALELHPPAHE-DPLFAGLPPQFPAHATHLQTVLRA--PDGAVVLARS 166
Cdd:PRK08007  73 LPILGVCLGHQAMAQAFGGKV-----VRAAKVMHGKTSPITHNgEGVFRGLANPLTVTRYHSLVVEPDslPACFEVTAWS 147

                         90       100
                 ....*....|....*....|....*
gi 499349865 167 PQDQCHAFRwgQSTW---GVQFHPE 188
Cdd:PRK08007 148 ETREIMGIR--HRQWdleGVQFHPE 170
PRK08857 PRK08857
aminodeoxychorismate/anthranilate synthase component II;
90-110 8.75e-03

aminodeoxychorismate/anthranilate synthase component II;


Pssm-ID: 181566 [Multi-domain]  Cd Length: 193  Bit Score: 36.39  E-value: 8.75e-03
                         10        20
                 ....*....|....*....|.
gi 499349865  90 MPLLGICYGHQLIAHALGGQV 110
Cdd:PRK08857  73 LPILGVCLGHQAIAQVFGGQV 93
 
Blast search parameters
Data Source: Precalculated data, version = cdd.v.3.21
Preset Options:Database: CDSEARCH/cdd   Low complexity filter: no  Composition Based Adjustment: yes   E-value threshold: 0.01

References:

  • Wang J et al. (2023), "The conserved domain database in 2023", Nucleic Acids Res.51(D)384-8.
  • Lu S et al. (2020), "The conserved domain database in 2020", Nucleic Acids Res.48(D)265-8.
  • Marchler-Bauer A et al. (2017), "CDD/SPARCLE: functional classification of proteins via subfamily domain architectures.", Nucleic Acids Res.45(D)200-3.
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